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TitleERK1/2 interaction with DHPS regulates eIF5A deoxyhypusination independently of ERK kinase activity.
Journal, issue, pagesCell Rep, Vol. 43, Issue 10, Page 114831, Year 2024
Publish dateOct 9, 2024
AuthorsAndrew E Becker / Paweł Kochanowski / Pui-Kei Wu / Elżbieta Wątor / Wenjing Chen / Koushik Guchhait / Artur P Biela / Przemysław Grudnik / Jong-In Park /
PubMed AbstractThis study explores a non-kinase effect of extracellular regulated kinases 1/2 (ERK1/2) on the interaction between deoxyhypusine synthase (DHPS) and its substrate, eukaryotic translation initiation ...This study explores a non-kinase effect of extracellular regulated kinases 1/2 (ERK1/2) on the interaction between deoxyhypusine synthase (DHPS) and its substrate, eukaryotic translation initiation factor 5A (eIF5A). We report that Raf/MEK/ERK activation decreases the DHPS-ERK1/2 interaction while increasing DHPS-eIF5A association in cells. We determined the cryoelectron microscopy (cryo-EM) structure of the DHPS-ERK2 complex at 3.5 Å to show that ERK2 hinders substrate entrance to the DHPS active site, subsequently inhibiting deoxyhypusination in vitro. In cells, impairing the ERK2 activation loop, but not the catalytic site, prolongs the DHPS-ERK2 interaction irrespective of Raf/MEK signaling. The ERK2 Ser-Pro-Ser motif, but not the common docking or F-site recognition sites, also regulates this complex. These data suggest that ERK1/2 dynamically regulate the DHPS-eIF5A interaction in response to Raf/MEK activity, regardless of its kinase function. In contrast, ERK1/2 kinase activity is necessary to regulate the expression of DHPS and eIF5A. These findings highlight an ERK1/2-mediated dual kinase-dependent and -independent regulation of deoxyhypusination.
External linksCell Rep / PubMed:39392755 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 6.66 Å
Structure data

17972

8pvu

EMDB-17972, PDB-8pvu:
Cryo-EM structure of DHS-ERK2 complex with 1:1 stoichiometry refined in C1 symmetry
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-17977: Cryo-EM structure of the third of three possible DHS-ERK2 complexes with 1:2 stoichiometry refined in C1 symmetry
Method: EM (single particle) / Resolution: 3.99 Å

EMDB-17978: Cryo-EM structure of the third of three possible DHS-ERK2 complexes with 1:2 stoichiometry refined in C2 symmetry
Method: EM (single particle) / Resolution: 3.78 Å

EMDB-17981: Cryo-EM structure of the second of three possible DHS-ERK2 complexes with 1:2 stoichiometry refined in C1 symmetry
Method: EM (single particle) / Resolution: 3.82 Å

EMDB-17982: Cryo-EM structure of the second of three possible DHS-ERK2 complexes with 1:2 stoichiometry refined in C2 symmetry
Method: EM (single particle) / Resolution: 3.71 Å

EMDB-17983: Cryo-EM structure of the first of three possible DHS-ERK2 complexes with 1:2 stoichiometry refined in C1 symmetry
Method: EM (single particle) / Resolution: 3.95 Å

EMDB-17984: Cryo-EM structure of the first of three possible DHS-ERK2 complexes with 1:2 stoichiometry refined in C2 symmetry
Method: EM (single particle) / Resolution: 3.74 Å

EMDB-17985: Cryo-EM structure of DHS-ERK2 complex with 1:3 stoichiometry refined in C1 symmetry
Method: EM (single particle) / Resolution: 3.67 Å

EMDB-17986: Cryo-EM structure of DHS-ERK2 complex with 1:4 stoichiometry refined in C1 symmetry
Method: EM (single particle) / Resolution: 6.66 Å

EMDB-17987: Cryo-EM structure of DHS-ERK2 complex with 1:4 stoichiometry refined in D2 symmetry
Method: EM (single particle) / Resolution: 4.54 Å

Source
  • homo sapiens (human)
KeywordsTRANSLATION / hypusination / transferase / protein-protein interaction / ERK1/2 kinase-independent function

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